This Article Full Text (PDF) Other Versions of this Article: JB.01326-07v1 190/3/1141    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Beláová, M. Articles by Mikuová, K. Search for Related Content PubMed PubMed Citation Articles by Beláová, M. Articles by Mikuová, K.

 Previous Article  |  Next Article 

J. Bacteriol. doi:10.1128/JB.01326-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Galactosyl Transferases in Mycobacterial Cell Wall Synthesis

Martina Beláová, Petronela Dianiková, Patrick J. Brennan^*, Gladys C. Completo, Natisha L. Rose, Todd L. Lowary, and Katarína Mikuová^*

Department of Biochemistry, Comenius University, Faculty of Natural Sciences, Bratislava, Slovakia, SK-842 15, Mycobacterial Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, U.S.A., CO 80523, Alberta Ingenuity Centre for Carbohydrate Science and Department of Chemistry, The University of Alberta, Edmonton, Canada, AB T6G 2G2

^* To whom correspondence should be addressed. Email: patrick.brennan{at}colostate.edu. mikusova{at}fns.uniba.sk.

	Abstract

Two galactosyltransferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Galf) acceptors that the recombinant galactofuranosyl transferase, GlfT1, from Mycobacterium smegmatis, the M. tuberculosis Rv3782 ortholog, known to be involved in the initial steps of galactan formation, harbors dual -(14) and -(15) Galf transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-GalfGalf, serves as a direct substrate for full polymerization catalyzed by another bifunctional Galf transferase, the GlfT2, the Rv3808c enzyme.